Known potent peptide caspase inhibitors (e.g. the irreversible pan-caspase inhibitor Z-VAD-fmk) [1,6] are only moderately selective and possess only poor cell permeabilities hindering the intracellular targeting of activated caspases [1,7]. In contrast, the 5-pyrrolidinylsulfonyl isatins represent a rare class of non-peptidyl caspase inhibitors which bind selectively to the downstream caspases, preferably to the effector caspases 3 and 7 [19]. The dicarbonyl functionality of the isatins bind in a tetrahedral manner to the caspase active site. A thiohemiketal is formed via the electrophilic C-3 carbonyl of the isatin and the nucleophilic thiolate function of the Cys163 residue of the enzyme. Consequently, the ability of the caspases to cleave substrates possessing a P1 Asp residue that reaches into the primary S1 pocket is blocked (reversible inhibitory effect) [20]. In contrast to the peptidomimetic caspase inhibitors, the 5-pyrrolidinylsulfonyl isatins do not possess an acidic functionality which may bind in the primary Asp binding pocket. Various N-substituted 5-pyrrolidinylsulfonyl isatins with the general formula 1 have been synthesized and disclosed so far [20-22]. Compounds bearing an allyl-, cyclohexylalkyl- or arylalkyl substituent at the N-1 nitrogen of the isatin are highly affine caspase 3 and 7 inhibiting agents. Their potency was proved by in vitro inhibition of recombinant human caspase 3 and 7 using standard fluorometric assays [21]. As recently described a non-peptidyl 5-pyrrolidinylsulfonyl isatin derivative was shown to possess cardioprotective potential in isolated rabbit hearts after ischemic injury as well as in cardiomyocytes [17].